NUCLEOPROTEIN PHOSPHORYLATED ON BOTH SERINE AND THREONINE IS PREFERENTIALLY ASSEMBLED INTO THE NUCLEOCAPSIDS OF MEASLES-VIRUS

The nucleoprotein (N) in the nucleocapsids of measles virus (MV) has different conformation and antigenicity than the free N-protein in MV-infected cells. These two forms of N-protein have identical methionine-containing tryptic peptides. The free N-protein contains 4 phosphorylated tryptic peptides. However, the nucleocapsid-associated N-protein has an additional phosphorylated peptide not found in the free N-protein. The free N-protein is phosphorylated only on serine residues, whereas the nucleocapsid-associated N-protein is phosphorylated on both serine and threonine residues. The MV N-protein expressed from a cloned gene in primate cells is also phosphorylated on both serine and threonine residues. These results suggest that cellular kinases phosphorylate the MV N-protein, and N-protein with phosphorylated serine and threonine is preferentially assembled into the viral nucleocapsids.